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Abstract

CLONING, EXPRESSION IN E.coli AND THE ENZYMATIC PROPERTIES OF LACCASE FROM Hypsizygus ulmarius

G. Ravikumar, M. Kalaiselvi, D. Gomathi, K. Devaki and C. Uma*

ABSTRACT

In the present study a laccase from Hypsizygus ulmarius was cloned and expressed in E.coli (BL 21). The laccase gene (1.6 Kb) which was isolated from the mushroom Hypsizygus ulmarius was successfully cloned to pET-29a (+) and expressed in E coli. The sequencing results confirmed the expression of the gene with 98% homology to that of the original gene as retrieved from NCBI. The recombinant laccase was produced from the transformed colonies and it was purified upto 23 fold with 51% recovery. The optimum pH and temperature for the purified laccase was found to be 6.0 and 40oC respectively. The molecular weight of the enzyme was found to be 63kDa. The enzyme activity was enhanced by the metal ions Mn2+and Cu2+ whereas it was reduced by Fe2+, Na2+ and Co2+. These results suggest that the recombinant laccase purified from the mushroom Hypsizygus ulmarius can be used for various biotechnological applications.

Keywords: Recombinant laccase, Hypsizygus ulmarius, E.coli.


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